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Q12874

- SF3A3_HUMAN

UniProt

Q12874 - SF3A3_HUMAN

Protein

Splicing factor 3A subunit 3

Gene

SF3A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri406 – 43732Matrin-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-splice site recognition Source: HGNC
    3. mRNA processing Source: HGNC
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. RNA splicing Source: Reactome
    6. RNA splicing, via transesterification reactions Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor 3A subunit 3
    Alternative name(s):
    SF3a60
    Spliceosome-associated protein 61
    Short name:
    SAP 61
    Gene namesi
    Name:SF3A3
    Synonyms:SAP61
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10767. SF3A3.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. nuclear speck Source: UniProtKB-SubCell
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. spliceosomal complex Source: HGNC

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35685.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501Splicing factor 3A subunit 3PRO_0000174318Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Glycosylationi119 – 1191N-linked (GlcNAc...)1 Publication
    Modified residuei299 – 2991Phosphoserine1 Publication
    Modified residuei365 – 3651Phosphoserine3 Publications
    Modified residuei367 – 3671Phosphoserine3 Publications
    Modified residuei369 – 3691Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ12874.
    PaxDbiQ12874.
    PeptideAtlasiQ12874.
    PRIDEiQ12874.

    PTM databases

    PhosphoSiteiQ12874.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ12874.
    BgeeiQ12874.
    CleanExiHS_SF3A3.
    GenevestigatoriQ12874.

    Organism-specific databases

    HPAiHPA032054.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A1, through its N-terminal region.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORFQ9Q2G43EBI-1051880,EBI-6248094From a different organism.
    SF3A1Q154592EBI-1051880,EBI-1054743

    Protein-protein interaction databases

    BioGridi116146. 63 interactions.
    DIPiDIP-882N.
    IntActiQ12874. 14 interactions.
    MINTiMINT-1467744.
    STRINGi9606.ENSP00000362110.

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi80 – 9617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DT7NMR-A71-107[»]
    ProteinModelPortaliQ12874.
    SMRiQ12874. Positions 71-107.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12874.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi354 – 3629Poly-Glu

    Sequence similaritiesi

    Belongs to the SF3A3 family.Curated
    Contains 1 matrin-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri406 – 43732Matrin-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5188.
    HOGENOMiHOG000160935.
    HOVERGENiHBG054452.
    InParanoidiQ12874.
    KOiK12827.
    OMAiYLDLHEC.
    OrthoDBiEOG77HDDF.
    PhylomeDBiQ12874.
    TreeFamiTF315227.

    Family and domain databases

    InterProiIPR024598. DUF3449.
    IPR021966. SF3a60_bindingd.
    IPR015880. Znf_C2H2-like.
    IPR000690. Znf_C2H2_matrin.
    [Graphical view]
    PfamiPF11931. DUF3449. 1 hit.
    PF12108. SF3a60_bindingd. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    PROSITEiPS50171. ZF_MATRIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12874-1 [UniParc]FASTAAdd to Basket

    « Hide

    METILEQQRR YHEEKERLMD VMAKEMLTKK STLRDQINSD HRTRAMQDRY    50
    MEVSGNLRDL YDDKDGLRKE ELNAISGPNE FAEFYNRLKQ IKEFHRKHPN 100
    EICVPMSVEF EELLKARENP SEEAQNLVEF TDEEGYGRYL DLHDCYLKYI 150
    NLKASEKLDY ITYLSIFDQL FDIPKERKNA EYKRYLEMLL EYLQDYTDRV 200
    KPLQDQNELF GKIQAEFEKK WENGTFPGWP KETSSALTHA GAHLDLSAFS 250
    SWEELASLGL DRLKSALLAL GLKCGGTLEE RAQRLFSTKG KSLESLDTSL 300
    FAKNPKSKGT KRDTERNKDI AFLEAQIYEY VEILGEQRHL THENVQRKQA 350
    RTGEEREEEE EEQISESESE DEENEIIYNP KNLPLGWDGK PIPYWLYKLH 400
    GLNINYNCEI CGNYTYRGPK AFQRHFAEWR HAHGMRCLGI PNTAHFANVT 450
    QIEDAVSLWA KLKLQKASER WQPDTEEEYE DSSGNVVNKK TYEDLKRQGL 500
    L 501
    Length:501
    Mass (Da):58,849
    Last modified:November 1, 1996 - v1
    Checksum:i6E6F6EA17777E1E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761E → G in CAA57388. (PubMed:7816610)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08815 mRNA. Translation: AAA19625.1.
    X81789 mRNA. Translation: CAA57388.1.
    AL603790 Genomic DNA. Translation: CAH69930.1.
    CH471059 Genomic DNA. Translation: EAX07304.1.
    CH471059 Genomic DNA. Translation: EAX07305.1.
    BC002395 mRNA. Translation: AAH02395.1.
    BC011523 mRNA. Translation: AAH11523.1.
    CCDSiCCDS428.1.
    PIRiA55749.
    RefSeqiNP_006793.1. NM_006802.2.
    UniGeneiHs.77897.

    Genome annotation databases

    EnsembliENST00000373019; ENSP00000362110; ENSG00000183431.
    GeneIDi10946.
    KEGGihsa:10946.
    UCSCiuc001cci.3. human.

    Polymorphism databases

    DMDMi17380310.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08815 mRNA. Translation: AAA19625.1 .
    X81789 mRNA. Translation: CAA57388.1 .
    AL603790 Genomic DNA. Translation: CAH69930.1 .
    CH471059 Genomic DNA. Translation: EAX07304.1 .
    CH471059 Genomic DNA. Translation: EAX07305.1 .
    BC002395 mRNA. Translation: AAH02395.1 .
    BC011523 mRNA. Translation: AAH11523.1 .
    CCDSi CCDS428.1.
    PIRi A55749.
    RefSeqi NP_006793.1. NM_006802.2.
    UniGenei Hs.77897.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DT7 NMR - A 71-107 [» ]
    ProteinModelPortali Q12874.
    SMRi Q12874. Positions 71-107.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116146. 63 interactions.
    DIPi DIP-882N.
    IntActi Q12874. 14 interactions.
    MINTi MINT-1467744.
    STRINGi 9606.ENSP00000362110.

    PTM databases

    PhosphoSitei Q12874.

    Polymorphism databases

    DMDMi 17380310.

    Proteomic databases

    MaxQBi Q12874.
    PaxDbi Q12874.
    PeptideAtlasi Q12874.
    PRIDEi Q12874.

    Protocols and materials databases

    DNASUi 10946.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373019 ; ENSP00000362110 ; ENSG00000183431 .
    GeneIDi 10946.
    KEGGi hsa:10946.
    UCSCi uc001cci.3. human.

    Organism-specific databases

    CTDi 10946.
    GeneCardsi GC01M038422.
    HGNCi HGNC:10767. SF3A3.
    HPAi HPA032054.
    MIMi 605596. gene.
    neXtProti NX_Q12874.
    PharmGKBi PA35685.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5188.
    HOGENOMi HOG000160935.
    HOVERGENi HBG054452.
    InParanoidi Q12874.
    KOi K12827.
    OMAi YLDLHEC.
    OrthoDBi EOG77HDDF.
    PhylomeDBi Q12874.
    TreeFami TF315227.

    Enzyme and pathway databases

    Reactomei REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi SF3A3. human.
    EvolutionaryTracei Q12874.
    GeneWikii SF3A3.
    GenomeRNAii 10946.
    NextBioi 41589.
    PROi Q12874.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12874.
    Bgeei Q12874.
    CleanExi HS_SF3A3.
    Genevestigatori Q12874.

    Family and domain databases

    InterProi IPR024598. DUF3449.
    IPR021966. SF3a60_bindingd.
    IPR015880. Znf_C2H2-like.
    IPR000690. Znf_C2H2_matrin.
    [Graphical view ]
    Pfami PF11931. DUF3449. 1 hit.
    PF12108. SF3a60_bindingd. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    PROSITEi PS50171. ZF_MATRIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Specific protein-protein interactions between the essential mammalian spliceosome-associated proteins SAP 61 and SAP 114."
      Chiara M.D., Champion-Arnaud P., Buvoli M., Nadal-Ginard B., Reed R.
      Proc. Natl. Acad. Sci. U.S.A. 91:6403-6407(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix adenocarcinoma.
    2. "Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo."
      Kraemer A., Legrain P., Mulhauser F., Groening K., Brosi R., Bilbe G.
      Nucleic Acids Res. 22:5223-5228(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix adenocarcinoma.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye and Lung.
    6. Bienvenut W.V.
      Submitted (OCT-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-9; 265-273 AND 292-303, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    7. "Functional association of U2 snRNP with the ATP-independent spliceosomal complex E."
      Das R., Zhou Z., Reed R.
      Mol. Cell 5:779-787(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
    8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
      Tissue: Liver.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP."
      Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P., Muto Y., Yokoyama S.
      Structure 14:1677-1689(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 71-107 IN COMPLEX WITH SF3A1, SUBUNIT.

    Entry informationi

    Entry nameiSF3A3_HUMAN
    AccessioniPrimary (citable) accession number: Q12874
    Secondary accession number(s): D3DPT5, Q15460, Q5VT87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3